5II9

Monoclinic crystal structure of red abalone lysin at 2.11 A resolution

Summary for 5II9

• Entry DOI: 10.2210/pdb5ii9/pdb
• Related: 1LIS 1LYN 2LIS 2LYN 5II7 5II8 5IIA 5IIB
• Descriptor: Egg-lysin (2 entities in total)
• Functional Keywords: cell adhesion, fertilization, egg-sperm interaction, gamete recognition, egg-binding protein, acrosomal protein, egg coat penetration
• Biological source: Haliotis rufescens (California red abalone)
• Total number of polymer chains: 6
• Total formula weight: 98900.79

Authors

Sadat Al-Hosseini, H.,Raj, I.,Nishimura, K.,Jovine, L. (deposition date: 2016-03-01, release date: 2017-06-14, Last modification date: 2024-01-10)

Primary citation

Raj, I.,Sadat Al Hosseini, H.,Dioguardi, E.,Nishimura, K.,Han, L.,Villa, A.,de Sanctis, D.,Jovine, L.
Structural Basis of Egg Coat-Sperm Recognition at Fertilization.
Cell, 169:1315-1326.e17, 2017

PubMed Abstract: Recognition between sperm and the egg surface marks the beginning of life in all sexually reproducing organisms. This fundamental biological event depends on the species-specific interaction between rapidly evolving counterpart molecules on the gametes. We report biochemical, crystallographic, and mutational studies of domain repeats 1-3 of invertebrate egg coat protein VERL and their interaction with cognate sperm protein lysin. VERL repeats fold like the functionally essential N-terminal repeat of mammalian sperm receptor ZP2, whose structure is also described here. Whereas sequence-divergent repeat 1 does not bind lysin, repeat 3 binds it non-species specifically via a high-affinity, largely hydrophobic interface. Due to its intermediate binding affinity, repeat 2 selectively interacts with lysin from the same species. Exposure of a highly positively charged surface of VERL-bound lysin suggests that complex formation both disrupts the organization of egg coat filaments and triggers their electrostatic repulsion, thereby opening a hole for sperm penetration and fusion.

PubMed: 28622512
DOI: 10.1016/j.cell.2017.05.033

Experimental method

X-RAY DIFFRACTION (2.11 Å)